Analytical Data
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Gene name
ZNRF4
- Application
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Alternative Names
E3 ubiquitin-protein ligase ZNRF4. EC:2.3.2.27. Nixin. RING finger protein 204. RING-type E3 ubiquitin transferase ZNRF4. Zinc/RING finger protein 4
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8WWF5
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Expression Region
1-429 aa
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AA Sequence
MPLCRPEHLMPRASRVPVAASLPLSHAVIPTQLPSRSGHRPPGRPRRCPKASCLPPPVGPSSTQTAKRVTMGWPRPGQALVAVKALLVLSLLQVPAQAVVRAVLEDNSSSVDFADLPALFGVPLAPEGIRGYLMEVKPANACHPIEAPRLGNRSLGSIALIRHYDCTFDLKVLNAQRAGFEAAIVHNVHSDDLVSMTHVYEDLRGQIAIPSVFVSEAASQDLRVILGCNKSAHALLLPDDPPCHDLGCHPVLTVSWVLGCTLALVVSAFFVLNHLWLWAQACCSHRRPVKTSTCQKAQVRTFTWHNDLCAICLDEYEEGDQLKILPCSHTYHCKCIDPWFSQAPRRSCPVCKQSVAATEDSFDSTTYSFRDEDPSLPGHRPPIWAIQVQLRSRRLELLGRASPHCHCSTTSLEAEYTTVSSAPPEAPGQ
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Molecular Weight
73.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
ZNRF4, a member of the RING-type E3 ubiquitin ligase family, plays a crucial role in various cellular processes, including protein degradation, signal transduction, and cellular response to stress. Recent studies have highlighted its potential involvement in regulating key signaling pathways, such as the Wnt pathway, which is essential for embryonic development and tissue homeostasis. Dysregulation of ZNRF4 has been linked to several diseases, including cancer, making it a subject of significant interest in biomedical research. The functional characterization of ZNRF4, particularly through the expression of its recombinant protein, is vital for understanding its biological functions and interactions with other cellular proteins. This research aims to explore the enzymatic activity of ZNRF4 and its role in ubiquitination processes, providing insights into how it influences cellular dynamics and the potential therapeutic implications for diseases associated with its dysfunction. Furthermore, studying ZNRF4 can contribute to the broader understanding of E3 ubiquitin ligases in cellular regulation and their promise as targets for drug development.
